3lnm
F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channelF233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedVoltage sensors regulate the conformations of voltage-dependent ion channels and enzymes. Their nearly switchlike response as a function of membrane voltage comes from the movement of positively charged amino acids, arginine or lysine, across the membrane field. We used mutations with natural and unnatural amino acids, electrophysiological recordings, and x-ray crystallography to identify a charge transfer center in voltage sensors that facilitates this movement. This center consists of a rigid cyclic "cap" and two negatively charged amino acids to interact with a positive charge. Specific mutations induce a preference for lysine relative to arginine. By placing lysine at specific locations, the voltage sensor can be stabilized in different conformations, which enables a dissection of voltage sensor movements and their relation to ion channel opening. A gating charge transfer center in voltage sensors.,Tao X, Lee A, Limapichat W, Dougherty DA, MacKinnon R Science. 2010 Apr 2;328(5974):67-73. PMID:20360102[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Rattus norvegicus
- Dougherty, D A
- Lee, A
- Limapichat, W
- MacKinnon, R
- Tao, X
- Glycoprotein
- Ion transport
- Ionic channel
- Lipoprotein
- Membrane
- Membrane protein
- Nadp
- Palmitate
- Phosphoprotein
- Potassium
- Potassium channel
- Potassium transport
- Transmembrane
- Transport
- Transport protein
- Voltage-gated channel
- Voltage-gated potassium channel-beta subunit complex